ID SODM_RAOPL Reviewed; 170 AA.
AC P22799;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-MAY-2023, entry version 88.
DE RecName: Full=Superoxide dismutase [Fe];
DE EC=1.15.1.1;
DE Flags: Fragment;
GN Name=sodA;
OS Raoultella planticola (Klebsiella planticola).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX NCBI_TaxID=575;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-26.
RX PubMed=7764218; DOI=10.1271/bbb.57.1454;
RA Lee S.O., Kim S.W., Uno I., Lee T.H.;
RT "Direct sequencing of superoxide dismutase genes from two bacterial strains
RT amplified by polymerase chain reaction.";
RL Biosci. Biotechnol. Biochem. 57:1454-1460(1993).
RN [2]
RP PROTEIN SEQUENCE OF 2-16, SUBUNIT, AND CHARACTERIZATION.
RC STRAIN=ATCC 8329 / NBRC 3317 / NCIB 8153;
RX PubMed=1368658; DOI=10.1271/bbb1961.55.101;
RA Kim S.W., Lee S.O., Lee T.H.;
RT "Purification and characterization of superoxide dismutase from Aerobacter
RT aerogenes.";
RL Agric. Biol. Chem. 55:101-108(1991).
CC -!- FUNCTION: Destroys superoxide anion radicals which are normally
CC produced within the cells and which are toxic to biological systems.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 1 Fe cation per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:1368658}.
CC -!- SIMILARITY: Belongs to the iron/manganese superoxide dismutase family.
CC {ECO:0000305}.
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DR PIR; PN0615; PN0615.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.990; Fe,Mn superoxide dismutase (SOD) domain; 1.
DR Gene3D; 3.55.40.20; Iron/manganese superoxide dismutase, C-terminal domain; 1.
DR InterPro; IPR001189; Mn/Fe_SOD.
DR InterPro; IPR019833; Mn/Fe_SOD_BS.
DR InterPro; IPR019832; Mn/Fe_SOD_C.
DR InterPro; IPR019831; Mn/Fe_SOD_N.
DR InterPro; IPR036324; Mn/Fe_SOD_N_sf.
DR InterPro; IPR036314; SOD_C_sf.
DR PANTHER; PTHR43595; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43595:SF2; 37S RIBOSOMAL PROTEIN S26, MITOCHONDRIAL; 1.
DR Pfam; PF02777; Sod_Fe_C; 1.
DR Pfam; PF00081; Sod_Fe_N; 1.
DR PIRSF; PIRSF000349; SODismutase; 1.
DR PRINTS; PR01703; MNSODISMTASE.
DR SUPFAM; SSF54719; Fe,Mn superoxide dismutase (SOD), C-terminal domain; 1.
DR SUPFAM; SSF46609; Fe,Mn superoxide dismutase (SOD), N-terminal domain; 1.
DR PROSITE; PS00088; SOD_MN; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Iron; Metal-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1368658,
FT ECO:0000269|PubMed:7764218"
FT CHAIN 2..>170
FT /note="Superoxide dismutase [Fe]"
FT /id="PRO_0000160036"
FT BINDING 27
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT NON_TER 170
SQ SEQUENCE 170 AA; 18468 MW; 7DE4F44E733EA16D CRC64;
MAYELPQLPY AYDALEPHID AKTXEIHHSK HHNTYVTNLN AAVEGTEFAD KDINDLIAML
DALPADKQTA VRNNGGGHAN HTLFWEVIAP GGSNTPVGEV AKAIDAKFGS FDAFKEEFAK
AATTRFGSGW AWLIVDGDSV AVTSTPNQDS PVMEGKTPVL GLDVWEHAYY
//
